ID   PNPP_SCHPO              Reviewed;         298 AA.
AC   Q00472; O74320;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=4-nitrophenylphosphatase;
DE            Short=PNPPase;
DE            EC=3.1.3.41;
GN   Name=pho2; ORFNames=SPBC15D4.15;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BD31;
RX   PubMed=1645660; DOI=10.1111/j.1432-1033.1991.tb16041.x;
RA   Yang J., Dhamija S.S., Schweingruber M.E.;
RT   "Characterisation of the specific p-nitrophenylphosphatase gene and protein
RT   of Schizosaccharomyces pombe.";
RL   Eur. J. Biochem. 198:493-497(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-nitrophenyl phosphate + H2O = 4-nitrophenol + H(+) +
CC         phosphate; Xref=Rhea:RHEA:21664, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57917,
CC         ChEBI:CHEBI:61146; EC=3.1.3.41;
CC   -!- ACTIVITY REGULATION: Activity enhanced by Mg(2+) ion but inhibited by
CC       Zn(2+) ion.
CC   -!- SUBUNIT: Homodimer.
CC   -!- PTM: The N-terminus is blocked.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X62722; CAA44597.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA20490.1; -; Genomic_DNA.
DR   PIR; S16088; S16088.
DR   PIR; T39491; T39491.
DR   RefSeq; NP_596255.1; NM_001022174.2.
DR   AlphaFoldDB; Q00472; -.
DR   SMR; Q00472; -.
DR   BioGRID; 276504; 50.
DR   STRING; 4896.SPBC15D4.15.1; -.
DR   MaxQB; Q00472; -.
DR   PaxDb; Q00472; -.
DR   PRIDE; Q00472; -.
DR   EnsemblFungi; SPBC15D4.15.1; SPBC15D4.15.1:pep; SPBC15D4.15.
DR   GeneID; 2539960; -.
DR   KEGG; spo:SPBC15D4.15; -.
DR   PomBase; SPBC15D4.15; pho2.
DR   VEuPathDB; FungiDB:SPBC15D4.15; -.
DR   eggNOG; KOG2882; Eukaryota.
DR   HOGENOM; CLU_043473_0_0_1; -.
DR   InParanoid; Q00472; -.
DR   OMA; PPMHRET; -.
DR   PhylomeDB; Q00472; -.
DR   PRO; PR:Q00472; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IDA:PomBase.
DR   GO; GO:0016791; F:phosphatase activity; IDA:PomBase.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IBA:GO_Central.
DR   GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006349; PGP_euk.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01452; PGP_euk; 1.
PE   4: Predicted;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..298
FT                   /note="4-nitrophenylphosphatase"
FT                   /id="PRO_0000058480"
FT   CONFLICT        1..49
FT                   /note="MAKKLSSPKEYKEFIDKFDVFLFDCDGVLWSGSKPIPGVTDTMKLLRSL ->
FT                   MKLLRSLGKSLLFFRVNSFT (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="L -> V (in Ref. 1; CAA44597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   298 AA;  32794 MW;  AEF1CF3DFD2D7435 CRC64;
     MAKKLSSPKE YKEFIDKFDV FLFDCDGVLW SGSKPIPGVT DTMKLLRSLG KQIIFVSNNS
     TKSRETYMNK INEHGIAAKL EEIYPSAYSS ATYVKKVLKL PADKKVFVLG EAGIEDELDR
     VGVAHIGGTD PSLRRALASE DVEKIGPDPS VGAVLCGMDM HVTYLKYCMA FQYLQDPNCA
     FLLTNQDSTF PTNGKFLPGS GAISYPLIFS TGRQPKILGK PYDEMMEAII ANVNFDRKKA
     CFVGDRLNTD IQFAKNSNLG GSLLVLTGVS KEEEILEKDA PVVPDYYVES LAKLAETA